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Database: UniProt
Entry: B0RES6
LinkDB: B0RES6
Original site: B0RES6 
ID   UVRB_CLAMS              Reviewed;         688 AA.
AC   B0RES6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   18-SEP-2019, entry version 86.
DE   RecName: Full=UvrABC system protein B {ECO:0000255|HAMAP-Rule:MF_00204};
DE            Short=Protein UvrB {ECO:0000255|HAMAP-Rule:MF_00204};
DE   AltName: Full=Excinuclease ABC subunit B {ECO:0000255|HAMAP-Rule:MF_00204};
GN   Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204};
GN   OrderedLocusNames=CMS1994;
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM
OS   20744 / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=31964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX   PubMed=18192393; DOI=10.1128/jb.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis
RT   subsp. sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. A damage recognition complex composed
CC       of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon
CC       binding of the UvrA(2)B(2) complex to a putative damaged site, the
CC       DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP
CC       binding by UvrB and probably causes local melting of the DNA
CC       helix, facilitating insertion of UvrB beta-hairpin between the DNA
CC       strands. Then UvrB probes one DNA strand for the presence of a
CC       lesion. If a lesion is found the UvrA subunits dissociate and the
CC       UvrB-DNA preincision complex is formed. This complex is
CC       subsequently bound by UvrC and the second UvrB is released. If no
CC       lesion is found, the DNA wraps around the other UvrB subunit that
CC       will check the other stand for damage. {ECO:0000255|HAMAP-
CC       Rule:MF_00204}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC       lesions. Interacts with UvrC in an incision complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00204}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}.
CC   -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC       {ECO:0000255|HAMAP-Rule:MF_00204}.
CC   -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00204}.
DR   EMBL; AM849034; CAQ02091.1; -; Genomic_DNA.
DR   RefSeq; WP_012299322.1; NZ_MZMN01000003.1.
DR   SMR; B0RES6; -.
DR   STRING; 31964.CMS1994; -.
DR   PRIDE; B0RES6; -.
DR   EnsemblBacteria; CAQ02091; CAQ02091; CMS1994.
DR   GeneID; 29470528; -.
DR   KEGG; cms:CMS1994; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   Proteomes; UP000001318; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00204; UvrB; 1.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   InterPro; IPR036876; UVR_dom_sf.
DR   InterPro; IPR004807; UvrB.
DR   InterPro; IPR041471; UvrB_inter.
DR   InterPro; IPR024759; UvrB_YAD/RRR_dom.
DR   PANTHER; PTHR24029; PTHR24029; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF02151; UVR; 1.
DR   Pfam; PF12344; UvrB; 1.
DR   Pfam; PF17757; UvrB_inter; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00631; uvrb; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW   DNA repair; Excision nuclease; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome; SOS response.
FT   CHAIN         1    688       UvrABC system protein B.
FT                                /FTId=PRO_1000077876.
FT   DOMAIN       31    188       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      434    587       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      642    677       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      44     51       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        97    120       Beta-hairpin.
SQ   SEQUENCE   688 AA;  77413 MW;  ACE600B1BE65E192 CRC64;
     MQPTRSVRPF KVVSDYSPSG DQPTAIAELA GRVNAGEPDV VLLGATGTGK SATAAWLIEK
     VQRPTLILAH NKTLAAQLAT EFRELMPDNA VEYFVSYYDY YQPEAYVPQT DTFIEKDSSV
     NAEVERLRHS TTNSLLSRRD VVVVSTVSCI YGLGQPEQYM NAMVALQVGM QINRDTLIRK
     FVSMQYQRND VDFSRGNFRV RGDTIEIIPM YEELAIRIEM FGDEIEALYQ LHPLTGDVVR
     KMDAVSVFPG SHYVAETEVM QRAIGTIQQE LEERLAVLER EGKLLEAQRL RMRTNFDIEM
     MQQIGFCSGI ENYSRHIDGR DAGEAPHCLL DYFPDDFLVV IDESHVTVPQ IGAMFEGDSS
     RKRTLVEHGF RLPSALDNRP LKWNEFTERV PQTVYMSATP GKYELGMGDG VVEQIIRPTG
     LIDPAIVVKP TKGQIDDLLE QIRIRVEKDE RILVTTLTKK MAEELTDYFA EAGVRVRYLH
     SDVDTLRRVE LLSELRAGVY DVLVGINLLR EGLDLPEVSL VAILDADKEG FLRSSTSLIQ
     TIGRAARNVS GEVHMYADVL TDSMKRAIEE TDRRREKQVA YNTEHGIDPT PLRKRIADIT
     EILAREGEDT KKMLEGRGGG KRSPTPNLRR EGKAAAGANE LETIISDLND QMLQAAGELK
     FELAARLRDE LGDLKRELRQ MEKAGHLS
//
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